Highlight | Nuclear Toxicology
A team at the Chemistry and Biology of Metals laboratory determined the cadmium interaction sites on CadA. CadA belongs to a family of ATPases called transporters P-type localized in cell membranes. Some of which are responsible for the cadmium resistance in bacteria. The results have shown that the CadA amino acids involved in the transport of cadmium belong to structures that pass through the membrane, four transmembrane helices.
These data were obtained as part of ToxNuc-E program.
Wu CC, Gardarin A, Martel A, Mintz E, Guillain F and Catty P
The cadmium transport sites of CadA, the Cd2+-ATPase from Listeria monocytogenes.
Journal of Biological Chemistry, 2006
Wu CC, Gardarin A, Catty P, Guillain F and Mintz E
CadA, the Cd2+-ATPase from Listeria monocytogenes, can use Cd2+ as co-substrate.
Banci L, Bertini I, Ciofi-Baffoni S, Su XC, Miras R, Bal N, Mintz E, Catty P, Shokes JE and Scott RA
Structural basis for metal binding specificity: The N-terminal cadmium binding domain of the P1-type ATPase CadA.
Journal of Molecular Biology, 2006
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